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Pre-replication Complex
A pre-replication complex (pre-RC) is a protein complex that forms at the origin of replication during the initiation step of DNA replication. Formation of the pre-RC is required for DNA replication to occur. Complete and faithful replication of the genome ensures that each daughter cell will carry the same genetic information as the parent cell. Accordingly, formation of the pre-RC is a very important part of the cell cycle. Components As organisms evolved and became increasingly more complex, so did their pre-RCs. The following is a summary of the components of the pre-RC amongst the different domains of life. In bacteria, the main component of the pre-RC is DnaA. The pre-RC is complete when DnaA occupies all of its binding sites within the bacterial origin of replication ( oriC). The archaeal pre-RC is very different from the bacterial pre-RC and can serve as a simplified model of the eukaryotic pre-RC. It is composed of a single origin recognition complex (ORC) protein, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Xenopus Laevis
The African clawed frog (''Xenopus laevis'', also known as the xenopus, African clawed toad, African claw-toed frog or the ''platanna'') is a species of African aquatic frog of the family Pipidae. Its name is derived from the three short claws on each hind foot, which it uses to tear apart its food. The word ''Xenopus'' means 'strange foot' and ''laevis'' means 'smooth'. The species is found throughout much of Sub-Saharan Africa (Nigeria and Sudan to South Africa),Weldon; du Preez; Hyatt; Muller; and Speare (2004). Origin of the Amphibian Chytrid Fungus.' Emerging Infectious Diseases 10(12). and in isolated, introduced populations in North America, South America, Europe, and Asia. All species of the family Pipidae are tongueless, toothless and completely aquatic. They use their hands to shove food in their mouths and down their throats and a hyobranchial pump to draw or suck things in their mouth. Pipidae have powerful legs for swimming and lunging after food. They also use t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
MCM10
Protein MCM10 homolog is a protein that in humans is encoded by the ''MCM10'' gene. It is essential for activation of the Cdc45: Mcm2-7:GINS helicase, and thus required for proper DNA replication. Function The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The protein complex formed by MCM proteins is a key component of the pre-replication complex (pre-RC) and it may be involved in the formation of replication forks and in the recruitment of other DNA replication related proteins. This protein can interact with MCM2 and MCM6, as well as with the origin recognition protein ORC2. It is regulated by proteolysis and phosphorylation in a cell cycle-dependent manner. Studies of a similar protein in Xenopus suggest that the chromatin binding of this protein at the onset of DNA replication is after pre-RC assembly and before origin unwinding. Alternatively splice ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
CDC7
Cell division cycle 7-related protein kinase is an enzyme that in humans is encoded by the ''CDC7'' gene. The Cdc7 kinase is involved in regulation of the cell cycle at the point of chromosomal DNA replication. The gene CDC7 appears to be conserved throughout eukaryotic evolution; this means that most eukaryotic cells have the Cdc7 kinase protein. Function The product encoded by this gene is predominantly localized in the nucleus and is a cell division cycle protein with kinase activity. The protein is a serine-threonine kinase that is activated by another protein called either Dbf4 in the yeast ''Saccharomyces cerevisiae'' or ASK in mammals. The Cdc7/Dbf4 complex adds a phosphate group to the minichromosome maintenance (MCM) protein complex allowing for the initiation of DNA replication in mitosis (as explained in the Cdc7 and Replication section below). Although expression levels of the protein appear to be constant throughout the cell cycle, the protein kinase activity app ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNA Polymerase
A DNA polymerase is a member of a family of enzymes that catalyze the synthesis of DNA molecules from nucleoside triphosphates, the molecular precursors of DNA. These enzymes are essential for DNA replication and usually work in groups to create two identical DNA duplexes from a single original DNA duplex. During this process, DNA polymerase "reads" the existing DNA strands to create two new strands that match the existing ones. These enzymes catalyze the chemical reaction : deoxynucleoside triphosphate + DNAn pyrophosphate + DNAn+1. DNA polymerase adds nucleotides to the three prime (3')-end of a DNA strand, one nucleotide at a time. Every time a cell divides, DNA polymerases are required to duplicate the cell's DNA, so that a copy of the original DNA molecule can be passed to each daughter cell. In this way, genetic information is passed down from generation to generation. Before replication can take place, an enzyme called helicase unwinds the DNA molecule from its t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Primase
DNA primase is an enzyme involved in the replication of DNA and is a type of RNA polymerase. Primase catalyzes the synthesis of a short RNA (or DNA in some living organisms) segment called a primer complementary to a ssDNA (single-stranded DNA) template. After this elongation, the RNA piece is removed by a 5' to 3' exonuclease and refilled with DNA. Function In bacteria, primase binds to the DNA helicase forming a complex called the primosome. Primase is activated by the helicase where it then synthesizes a short RNA primer approximately 11 ±1 nucleotides long, to which new nucleotides can be added by DNA polymerase. Archaeal and eukaryote primases are heterodimeric proteins with one large regulatory and one minuscule catalytic subunit. The RNA segments are first synthesized by primase and then elongated by DNA polymerase. Then the DNA polymerase forms a protein complex with two primase subunits to form the alpha DNA Polymerase primase complex. Primase is one of the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DnaG
DnaG is a bacterial DNA primase and is encoded by the ''dnaG'' gene. The enzyme DnaG, and any other DNA primase, synthesizes short strands of RNA known as oligonucleotides during DNA replication. These oligonucleotides are known as primers because they act as a starting point for DNA synthesis. DnaG catalyzes the synthesis of oligonucleotides that are 10 to 60 nucleotides (the fundamental unit of DNA and RNA) long, however most of the oligonucleotides synthesized are 11 nucleotides. These RNA oligonucleotides serve as primers, or starting points, for DNA synthesis by bacterial DNA polymerase III (Pol III). DnaG is important in bacterial DNA replication because DNA polymerase cannot initiate the synthesis of a DNA strand, but can only add nucleotides to a preexisting strand. DnaG synthesizes a single RNA primer at the origin of replication. This primer serves to prime leading strand DNA synthesis. For the other parental strand, the lagging strand, DnaG synthesizes an RNA prime ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Single-strand Binding Protein
Single-strand DNA-binding protein (SSB) is a protein found in ''Escherichia coli'' (''E. coli'') bacteria, that Single-stranded binding protein, binds to single-stranded regions of deoxyribonucleic acid (DNA). Single-stranded DNA is produced during all aspects of DNA metabolism: replication, recombination, and repair. As well as stabilizing this single-stranded DNA, SSB proteins bind to and modulate the function of numerous proteins involved in all of these processes. Active ''E. coli'' SSB is composed of four identical 19 Atomic mass unit, kDa subunits. Binding of single-stranded DNA to the tetramer can occur in different "modes", with SSB occupying different numbers of DNA bases depending on a number of factors, including salt concentration. For example, the (SSB)65 binding mode, in which approximately 65 nucleotides of DNA wrap around the SSB tetramer and contact all four of its subunits, is favoured at high salt concentrations ''in vitro''. At lower salt concentrations, the (SSB) ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DnaC
dnaC is a loading factor that complexes with the C-terminus of helicase dnaB and inhibits it from unwinding the dsDNA at a replication fork. A dnaB and dnaC associate near the dnaA bound origin for each of the ssDNA. One dnaB-dnaC complex is oriented in the opposite direction to the other dnaB-dnaC complex due to the antiparallel nature of DNA. Because they are oriented in opposite directions, one dnaB-dnaC complex will complex with dnaA from the N-terminus of dnaB whereas the other dnaB-dnaC complex will complex with dnaA from the dnaC. After the assembly of dnaG onto the N-terminus of dnaB, dnaC is released and dnaB will be allowed to begin unwinding dsDNA to make room for DNA polymerase III DNA polymerase III holoenzyme is the primary enzyme complex involved in prokaryotic DNA replication. It was discovered by Thomas Kornberg (son of Arthur Kornberg) and Malcolm Gefter in 1970. The complex has high processivity (i.e. the number of ... to begin synthesizing the daughter stra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DnaB Helicase
DnaB helicase is an enzyme in bacteria which opens the replication fork during DNA replication. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerisation of the N-terminal domain has been observed and may occur during the enzymatic cycle. Initially when DnaB binds to dnaA, it is associated with dnaC, a negative regulator. After DnaC dissociates, DnaB binds dnaG. The N-terminal has a multi-helical structure that forms an orthogonal bundle. The C-terminal domain contains an ATP-binding site and is therefore probably the site of ATP hydrolysis. In eukaryotes, helicase function is provided by the MCM ( Minichromosome maintenance) complex. The DnaB helicase is the product of the ''dnaB'' gene. The helicase enzyme that is produced is a hexamer in ''E. coli'', as well as in many other bacteria. The energy for DnaB activity is provide ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cyclin-dependent Kinase
Cyclin-dependent kinases (CDKs) are the families of protein kinases first discovered for their role in regulating the cell cycle. They are also involved in regulating transcription, mRNA processing, and the differentiation of nerve cells. They are present in all known eukaryotes, and their regulatory function in the cell cycle has been evolutionarily conserved. In fact, yeast cells can proliferate normally when their CDK gene has been replaced with the homologous human gene. CDKs are relatively small proteins, with molecular weights ranging from 34 to 40 kDa, and contain little more than the kinase domain. By definition, a CDK binds a regulatory protein called a cyclin. Without cyclin, CDK has little kinase activity; only the cyclin-CDK complex is an active kinase but its activity can be typically further modulated by phosphorylation and other binding proteins, like p27. CDKs phosphorylate their substrates on serines and threonines, so they are serine-threonine kinases. The ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
G1 Phase
The G1 phase, gap 1 phase, or growth 1 phase, is the first of four phases of the cell cycle that takes place in eukaryotic cell division. In this part of interphase, the cell synthesizes mRNA and proteins in preparation for subsequent steps leading to mitosis. G1 phase ends when the cell moves into the S phase of interphase. Around 30 to 40 percent of cell cycle time is spent in the G1 phase. Overview G1 phase together with the S phase and G2 phase comprise the long growth period of the cell cycle cell division called interphase that takes place before cell division in mitosis (M phase). During G1 phase, the cell grows in size and synthesizes mRNA and protein that are required for DNA synthesis. Once the required proteins and growth are complete, the cell enters the next phase of the cell cycle, S phase. The duration of each phase, including the G1 phase, is different in many different types of cells. In human somatic cells, the cell cycle lasts about 10 hours, and the G1 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
